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Database: UniProt/TrEMBL
Entry: R8BK14_TOGMI
LinkDB: R8BK14_TOGMI
Original site: R8BK14_TOGMI 
ID   R8BK14_TOGMI            Unreviewed;       552 AA.
AC   R8BK14;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   25-OCT-2017, entry version 25.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|RuleBase:RU361171};
GN   ORFNames=UCRPA7_4839 {ECO:0000313|EMBL:EON99624.1};
OS   Togninia minima (strain UCR-PA7) (Esca disease fungus)
OS   (Phaeoacremonium aleophilum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Togniniales; Togniniaceae;
OC   Phaeoacremonium.
OX   NCBI_TaxID=1286976 {ECO:0000313|EMBL:EON99624.1, ECO:0000313|Proteomes:UP000014074};
RN   [1] {ECO:0000313|Proteomes:UP000014074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCR-PA7 {ECO:0000313|Proteomes:UP000014074};
RX   PubMed=23814032; DOI=10.1128/genomeA.00390-13;
RA   Blanco-Ulate B., Rolshausen P., Cantu D.;
RT   "Draft genome sequence of the ascomycete Phaeoacremonium aleophilum
RT   strain UCR-PA7, a causal agent of the esca disease complex in
RT   grapevines.";
RL   Genome Announc. 1:E0039013-E0039013(2013).
CC   -!- CATALYTIC ACTIVITY: L-glutamate = 4-aminobutanoate + CO(2).
CC       {ECO:0000256|RuleBase:RU361171}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC         ECO:0000256|RuleBase:RU361171};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU361171}.
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DR   EMBL; KB933141; EON99624.1; -; Genomic_DNA.
DR   RefSeq; XP_007915581.1; XM_007917390.1.
DR   EnsemblFungi; EON99624; EON99624; UCRPA7_4839.
DR   GeneID; 19325331; -.
DR   KEGG; tmn:UCRPA7_4839; -.
DR   KO; K01580; -.
DR   OrthoDB; EOG092C1P0W; -.
DR   Proteomes; UP000014074; Unassembled WGS sequence.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:EnsemblFungi.
DR   GO; GO:0006538; P:glutamate catabolic process; IEA:EnsemblFungi.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR010107; Glutamate_decarboxylase.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   PANTHER; PTHR43321; PTHR43321; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 2.
DR   TIGRFAMs; TIGR01788; Glu-decarb-GAD; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000014074};
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|RuleBase:RU361171};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU361171};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014074}.
FT   MOD_RES     291    291       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR602129-50}.
SQ   SEQUENCE   552 AA;  61909 MW;  9F0D798D9F22ADB1 CRC64;
     MVLARHVDPE DVVSRLRDIH LAEPGHEGLR GQGGSQHLTP YMGTRYEAQM SIPKFKIPDD
     GAPSDTVYYM IKDDFVNTYG EANAQQLMIE NFAKNLADSD EYPAMLAIHD RCISILAHLW
     GVQSGEKAVG SATTGSSEAI HLGGLAMKRR WQEKRQAEGK DTLKPNIIMG SNAQVALEKF
     ARYFDVEARI LPVSAKSKFR LDPDLVRENI DENTIGIFVI LGSTYTGHYE PVEEISKILD
     EYQEKTGIDI PIHVDAASGG FVAPFTHCQA GGPKWNFELP RVKSINASGH KYGLVYAGVG
     WIVWRDESFL PQHLIFELHY LGGTEKSFTL NFSRPGAQVI VQYYNLIHLG FSGYREIMEN
     CLANARLLSN ALEETGWYHC VSDVHRKVSN PARIADTVKA AVSSAPETSA HYIASLPVVS
     FRFSDEFKKE YPHIKQENVS LLLRARQWII PNYALPPNED HTEILRVVIR ESMSFDLLDR
     LISDICQVTQ TLMDNDEVDL SVLHKNKRKV LLKSEQEAKK GDADKKRSGE RGKEIIGGET
     KKMAEGIHRS VC
//
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